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FSL1_GIBZE
ID   FSL1_GIBZE              Reviewed;        2642 AA.
AC   I1S166; A0A098DD60;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Fusarielin synthase FSL1 {ECO:0000303|PubMed:22252016};
DE            EC=2.3.1.- {ECO:0000305|PubMed:27983606};
DE   AltName: Full=Fusarielin biosynthesis cluster protein 1 {ECO:0000303|PubMed:22252016};
DE   AltName: Full=Reducing polyketide synthase FSL1 {ECO:0000303|PubMed:22252016};
GN   Name=FSL1 {ECO:0000303|PubMed:22252016};
GN   Synonyms=PKS9 {ECO:0000303|PubMed:22252016};
GN   ORFNames=FG10464, FGRAMPH1_01T08165;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
RN   [4]
RP   IDENTIFICATION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX   PubMed=16278459; DOI=10.1128/ec.4.11.1926-1933.2005;
RA   Gaffoor I., Brown D.W., Plattner R., Proctor R.H., Qi W., Trail F.;
RT   "Functional analysis of the polyketide synthase genes in the filamentous
RT   fungus Gibberella zeae (anamorph Fusarium graminearum).";
RL   Eukaryot. Cell 4:1926-1933(2005).
RN   [5]
RP   INDUCTION, FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=22252016; DOI=10.1111/j.1462-2920.2011.02696.x;
RA   Soerensen J.L., Hansen F.T., Sondergaard T.E., Staerk D., Lee T.V.,
RA   Wimmer R., Klitgaard L.G., Purup S., Giese H., Frandsen R.J.;
RT   "Production of novel fusarielins by ectopic activation of the polyketide
RT   synthase 9 cluster in Fusarium graminearum.";
RL   Environ. Microbiol. 14:1159-1170(2012).
RN   [6]
RP   INDUCTION.
RX   PubMed=23290226; DOI=10.1016/j.ijfoodmicro.2012.10.016;
RA   Soerensen J.L., Akk E., Thrane U., Giese H., Sondergaard T.E.;
RT   "Production of fusarielins by Fusarium.";
RL   Int. J. Food Microbiol. 160:206-211(2013).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=27983606; DOI=10.3390/molecules21121710;
RA   Droce A., Saei W., Joergensen S.H., Wimmer R., Giese H., Wollenberg R.D.,
RA   Sondergaard T.E., Soerensen J.L.;
RT   "Functional Analysis of the Fusarielin Biosynthetic Gene Cluster.";
RL   Molecules 21:0-0(2016).
CC   -!- FUNCTION: Reducing polyketide synthase; part of the gene cluster that
CC       mediates the biosynthesis of fusarielins F, G and H, decaketide
CC       compounds with 5 methylations and a decaline core that act as
CC       mycoestrogens as they stimulate growth of MCF-7 breast cancer cells
CC       (PubMed:22252016, PubMed:27983606). The initial compound in the pathway
CC       is produced by the reducing polyketide synthase FSL1. FSL1 lacks an
CC       active enoyl reductase (ER) domain and biosynthesis of fusarielins
CC       relies on the trans-acting enoyl reductase FSL5, before it is released
CC       through hydrolysis catalyzed by the thioesterase FSL2 (PubMed:22252016,
CC       PubMed:27983606). Fusarielins F, G, and H have a C11=C12 cis double
CC       bond and is fully reduced between C10 and C11 and between C12 and C13.
CC       FSL3 can be involved in the formation of the C11=C12 cis double bond by
CC       moving a hypothetical C10=C11 or C12=C13 trans double bond to form
CC       prefusarielin (PubMed:27983606). Prefusarielin is oxygenated at C15 and
CC       C16 by the cytochrome P450 monooxygenase FSL4, resulting in fusarielin
CC       F, which subsequently is epoxidized into fusarielin G by the same
CC       enzyme (PubMed:27983606). The final step in the pathway is a reduction
CC       of the carboxylic acid moiety to yield fusarielin H via a still
CC       undetermined mechanism (PubMed:27983606). {ECO:0000269|PubMed:22252016,
CC       ECO:0000269|PubMed:27983606}.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y8A5};
CC       Note=Binds 1 phosphopantetheine covalently.
CC       {ECO:0000250|UniProtKB:Q9Y8A5};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:22252016, ECO:0000269|PubMed:27983606}.
CC   -!- INDUCTION: Expressed during sexual development (PubMed:16278459). Is
CC       not expressed during infection of wheat plants (PubMed:23290226).
CC       Expression is positively regulated by the fusarielin biosynthesis
CC       cluster-specific transcription factor FSL7, probably via its binding at
CC       the 5'-CGGNNNCCG-3' motif present in the promoter of all the cluster
CC       genes (PubMed:22252016). {ECO:0000269|PubMed:16278459,
CC       ECO:0000269|PubMed:22252016, ECO:0000269|PubMed:23290226}.
CC   -!- DOMAIN: Multidomain protein; including a ketosynthase (KS) that
CC       catalyzes repeated decarboxylative condensation to elongate the
CC       polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects
CC       and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain
CC       that reduces hydroxyl groups to enoyl groups; a methyltransferase (MET)
CC       domain that transfers methyl groups to the growing polyketide; a
CC       ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and
CC       an acyl-carrier protein (ACP) that serves as the tether of the growing
CC       and completed polyketide via its phosphopantetheinyl arm (Probable).
CC       Lacks an active enoyl reductase (ER) domain that reduces enoyl groups
CC       to alkyl groups, and biosynthesis of fusarielins relies on the trans-
CC       acting enoyl reductase FSL5 (Probable). {ECO:0000305|PubMed:22252016}.
CC   -!- DISRUPTION PHENOTYPE: Leads to significant increase in growth
CC       (PubMed:16278459). Abolishes the production of fusarielins F, G and H
CC       (PubMed:22252016, PubMed:27983606). {ECO:0000269|PubMed:16278459,
CC       ECO:0000269|PubMed:22252016, ECO:0000269|PubMed:27983606}.
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DR   EMBL; HG970332; CEF75886.1; -; Genomic_DNA.
DR   RefSeq; XP_011319443.1; XM_011321141.1.
DR   AlphaFoldDB; I1S166; -.
DR   SMR; I1S166; -.
DR   STRING; 5518.FGSG_10464P0; -.
DR   GeneID; 23557369; -.
DR   KEGG; fgr:FGSG_10464; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G08165; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_37_5_1; -.
DR   InParanoid; I1S166; -.
DR   Proteomes; UP000070720; Chromosome 1.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.10.129.110; -; 1.
DR   Gene3D; 3.40.366.10; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020807; PKS_dehydratase.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW   Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..2642
FT                   /note="Fusarielin synthase FSL1"
FT                   /id="PRO_0000444959"
FT   DOMAIN          2556..2635
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:22252016"
FT   REGION          9..453
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:22252016"
FT   REGION          566..890
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:22252016"
FT   REGION          965..1279
FT                   /note="Dehydrogenase (DH) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:22252016"
FT   REGION          1423..1622
FT                   /note="Methyltransferase (MET) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:22252016"
FT   REGION          2244..2423
FT                   /note="Ketoreductase (KR) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:22252016"
FT   ACT_SITE        179
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        659
FT                   /note="For malonyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        997
FT                   /note="For beta-hydroxyacyl dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2595
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2642 AA;  286924 MW;  F23B2B3301E70356 CRC64;
     MQGPTNEPIA IIGTGCRFPG GSNTASKLWD LLKDPKDVSK EVPEDRFNLD RFYHKDSSHH
     GTANVRRSYL LDEDVRLFDT QFFGISPGEA QAMDPQHRVL LEVVYEAIES AGKTIHGLHN
     SDTAVYVGLM CTDYYVIQAA DLNSVPTYNA TGVANSNASS RVSYFFNWHG PSMTIDTACS
     SSLVAVHEAV QALRNGTSRM AVACGTNLIL SPLPFISESN LSMLSPTGKS RMWDADADGY
     ARGEGVAAVV LKPLSAAIED NDVIECIIRE VGVNQDGKTR GITMPSAQAQ ASLIRQTYAK
     AGLDPATPEG RCQFFEAHGT GTPAGDPQEA EALKTAFFPN ETDSVTNGTN GLLSEADNLL
     VGSIKTVIGH TEGTAGLAGL IKACMALKHG AVPPNLLFNR LNPALEPFTK HLSIPTSLTP
     WPTLLTNVPR RASVNSFGFG GTNAHAILEA YSQAPQNSFA TPSSSPLVVP AIPFVFSAAS
     ETSLRGVLES FLEYLNTSKD KDESLDLTSL AYILSTKRTV LSQRVSIIAS TFEQLLEKVE
     AVLDDSASSV VGSKAATLSH PALLGVFTGQ GAQWATMGTK LMRSNPLAQS VIQDLDAVLA
     SLPECHRPRW SLGRELLADT TSRIKEAELS QPLCTAVQIM LVDLLKANGV QFQGVVGHSS
     GEIAAAYAAG FVSSADAIKI AYYRGYFAKL ASGSSSTGKD SSVKGSMMAV GTTYEDAIEL
     CQLEDFRGRI SLAAHNGPNS VTLSGDSDAI NQAHFIFSEE EKKFARLLKV DTAYHSSHMQ
     PCVSPYTEAL QACGIVAREP ASDAPKWFSS VRSGKPVLDV DGLDCQYWVD NLLSPVMFHE
     AVQGCLDSSD TYNAILEIGP HAALKGPLDE SVLELMGNKL PYTSALVRGK DDIESFSTAL
     GFLWTQFGNQ CVDLGTFQKR VSKDTGSKLC STMDDLPTYA WTHDKPLWAE SRSTKLFRTM
     PGSFHDLLGI QTADGTAEEW RWQNILKTKE LPWMVGHALQ GQIVFPGTGY IALAMEASLQ
     IAQGRPVSKI DLYDLEIRKA IAVNESASGT ELLVTMTNVS AIHPDVETIT ADFATYSTIS
     RESGSMALNC CGKVCIFLQT ETVTTTGSDG HAAEQFATRS TPVPGMAGID VERFYSAMQH
     DLGYMYSGPF RGLSRLSRKL GFSEGSIQRP PFGEDGSETT LIFHPGMLDN ALQGLFAAYS
     APGDGRLWSM RAPTACRRVS LVPSLCGPNM TEEVDFDCTL TDSRDDFITG DVEVYASGYS
     QRIIEIEGLS FSPFAAATDR DDRQLFQEQI WCVNEADGPL VLGNMAPTFE ERTKALDAER
     AAFFYLKKLH LSVPSDQRSQ LPWYRQSLLD NAERLYDLVC SGTHSYAPQS WIQDTKEDVY
     AMMESYGPQD ADFNLTKAVG ENLPLPDVIK GDTNILQYMT QNNYLDRYYT HAIGFGWLNV
     LISGVVGQIA DKHPKMRFLE IGAGTGGATG AVLDRIGQAY SSYTYTDISS GFFERAVDKF
     QDHAGKMLFK MLDIEKDPVS QGFPEHSYDI ILAANVLHAT KNLTETLQNT RRLLKPGGFL
     VLMEILGNDV MRIGLVMGGL PGWWVGKDDG RRWGPTITLE EWDTLLKGTG FAGVDTNTPM
     PDKVQMPGSV FVAQAVDDRI VKLRDPLQHD ALPSAATDHV NGIQNGHTPS PTISKGTSHL
     VVIGGSSTSG SKLASDIIRV LSPLFAEIIH IPQLDSKDAI AKIPSNVDLH ILSLTECDTG
     GTFFHNISNT AWQNFQHLLA TSPASLLWVV PNTRSGNPLG AIGTGLFRSL FYEIPETKFQ
     VLDLDEKATG YLSGCAGLIA KLVQQLRLVT DTSSARGPST LTPETSEDDL QSVNDGTATV
     EMLWTVEPEL YLHDGRLYIS RVRLQKAQND RYNSWRRPIL QLTESKSTVD PSLSTSSLGR
     QTSLELQWKD DAYYNLKEIN WFAKPLSTDS ATIDVSCSLA SCLKTPAGFF FVQVGTDVNT
     GEKKLCLSTE NRSRVTVHSS WTETLKQEHD VADGQYMSFI VADMIVQQIM YMLPPTGILL
     LHEPDPGLAS LLTRQLANIG RKVVFTTTRS DKSTNLLSKA NWIFMHPRLN KRLIESALPH
     GVTFFIDCGQ AEDVIHEGSH GKDHGLGLRL HNSLSRTCVK RTLQDLTSRT ASVAPHEATG
     EVVKLLHRIT TFAAAQLNSV PDGAPLKVKS LSEIVSRAKT RALATAEGCS TGPFCLVNWH
     AESQVPISVA PVWDRDDLFR SDRTYWMLGL TGDLGRSLAE FMISRGARHV VLSSRTPQPD
     EMWVERQQKK YGATVVYIAV DLTSLDSVQK AHKQIVKSMP PLAGVANGAL VLKDSSVAKM
     TIEQLQAVLR PKVDGTLHLQ SVVDANSGSE EQPLDWFIAF SSIVGTTGNL GQAAYSAANG
     FLKAWVSQQR SMFGHNAAVI DISRVLGVGY VERETQSNSG RLTREQTDRL MNRTGTLAMS
     ETDLHQLFAE AVVAADHCSA SNTGLSVGAR DAEIITGIAP ISSAQAEDVF WARNPRFGLL
     VIDSNAAVGG DDQDGKGSER RQVPVKTQLA AANTPQEVTS VLTSCIVTKL RASLFLSASD
     SFSETVALVD QGVDSLVGVD IRTWCIKELD VDVPVLKILG GASVVDLADY ILESLPVKEK
     SK
 
 
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